{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bohlender LL"],"funding":["Deutsche Forschungsgemeinschaft","Albert-Ludwigs-Universität Freiburg im Breisgau"],"pagination":["45"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12852254"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["45(2)"],"pubmed_abstract":["<h4>Key message</h4>Scalable moss bioreactors enable the production of high-quality recombinant prolyl-hydroxylated human collagen without heterologous P4H expression, offering a sustainable and vegan alternative to conventional collagens derived from animals. Collagens are structural proteins of the extracellular matrix essential for skin elasticity and integrity. They are widely used in dietary supplements and cosmetics. Conventional collagens of animal origin raise concerns regarding ethics, safety, and sustainability. As a vegan alternative, we report on the production of a 30 kDa prolyl-hydroxylated human collagen polypeptide from Physcomitrella moss plants. For secretion-based production and formulation compatibility, a hydrophilic region encompassing 334 amino acids from human type "],"journal":["Plant cell reports"],"pubmed_title":["Secretion-based production of prolyl-hydroxylated human type III collagen in scalable Physcomitrella photobioreactors."],"pmcid":["PMC12852254"],"funding_grant_id":["CIBSS - EXC-2189 - Project ID 390939984","CIBSS – EXC-2189 – Project ID 390939984"],"pubmed_authors":["Mitgau A","Parsons J","Henes B","Decker EL","Hoernstein SNW","Grigolon G","Bohlender LL","Reski R"],"additional_accession":[]},"is_claimable":false,"name":"Secretion-based production of prolyl-hydroxylated human type III collagen in scalable Physcomitrella photobioreactors.","description":"<h4>Key message</h4>Scalable moss bioreactors enable the production of high-quality recombinant prolyl-hydroxylated human collagen without heterologous P4H expression, offering a sustainable and vegan alternative to conventional collagens derived from animals. Collagens are structural proteins of the extracellular matrix essential for skin elasticity and integrity. They are widely used in dietary supplements and cosmetics. Conventional collagens of animal origin raise concerns regarding ethics, safety, and sustainability. As a vegan alternative, we report on the production of a 30 kDa prolyl-hydroxylated human collagen polypeptide from Physcomitrella moss plants. For secretion-based production and formulation compatibility, a hydrophilic region encompassing 334 amino acids from human type ","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-07-15T18:08:26.41Z","creation":"2026-07-08T03:08:52.617Z"},"accession":"S-EPMC12852254","cross_references":{"pubmed":["41604015"],"doi":["10.1007/s00299-026-03727-7"]}}